5KX6
The structure of Arabidopsis thaliana FUT1 Mutant R284K in complex with GDP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-08-05 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.54178 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.224, 112.957, 87.824 |
Unit cell angles | 90.00, 104.48, 90.00 |
Refinement procedure
Resolution | 85.030 - 2.200 |
R-factor | 0.25631 |
Rwork | 0.253 |
R-free | 0.32726 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5koe |
RMSD bond length | 0.021 |
RMSD bond angle | 2.094 |
Data reduction software | PROTEUM PLUS |
Data scaling software | PROTEUM PLUS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 85.030 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.108 | 0.481 |
Number of reflections | 47518 | |
<I/σ(I)> | 6 | 1.14 |
Completeness [%] | 91.2 | 84.5 |
Redundancy | 2.71 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 7 mg/mL protein in 0.1 M MES pH 6.0 to 7.0 and 16% to 23% w/v PEG 3350 |